Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis

Masaaki K. Sato, Takashi Ishihara, Hiroto Tanaka, Akihiko Ishijima, Yuichi Inoue

研究成果: Article査読

7 被引用数 (Scopus)

抄録

The actomyosin interaction plays a key role in a number of cellular functions. Single-molecule measurement techniques have been developed to study the mechanism of the actomyosin contractile system. However, the behavior of isolated single molecules does not always reflect that of molecules in a complex system such as a muscle fiber. Here, we developed a simple method for studying the kinetic parameters of the actomyosin interaction using small numbers of molecules. This approach does not require the specialized equipment needed for single-molecule measurements, and permits us to observe behavior that is more similar to that of a complex system. Using an in vitro motility assay, we examined the duration of continuous sliding of actin filaments on a sparsely distributed heavy meromyosin-coated surface. To estimate the association rate constant of the actomyosin motile system, we compared the distribution of experimentally obtained duration times with a computationally simulated distribution. We found that the association rate constant depends on the sliding velocity of the actin filaments. This technique may be used to reveal new aspects of the kinetics of various motor proteins in complex systems.

本文言語English
ページ(範囲)711-718
ページ数8
ジャーナルBiophysical Journal
103
4
DOI
出版ステータスPublished - 2012 8 22

ASJC Scopus subject areas

  • 生物理学

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